NANE_STRP1
ID NANE_STRP1 Reviewed; 234 AA.
AC P65522; Q490Y7; Q9A1J0;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=Putative N-acetylmannosamine-6-phosphate 2-epimerase {ECO:0000255|HAMAP-Rule:MF_01235};
DE EC=5.1.3.9 {ECO:0000255|HAMAP-Rule:MF_01235};
DE AltName: Full=ManNAc-6-P epimerase {ECO:0000255|HAMAP-Rule:MF_01235};
GN Name=nanE {ECO:0000255|HAMAP-Rule:MF_01235};
GN OrderedLocusNames=SPy_0251, M5005_Spy0212;
OS Streptococcus pyogenes serotype M1.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=301447;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700294 / SF370 / Serotype M1;
RX PubMed=11296296; DOI=10.1073/pnas.071559398;
RA Ferretti J.J., McShan W.M., Ajdic D.J., Savic D.J., Savic G., Lyon K.,
RA Primeaux C., Sezate S., Suvorov A.N., Kenton S., Lai H.S., Lin S.P.,
RA Qian Y., Jia H.G., Najar F.Z., Ren Q., Zhu H., Song L., White J., Yuan X.,
RA Clifton S.W., Roe B.A., McLaughlin R.E.;
RT "Complete genome sequence of an M1 strain of Streptococcus pyogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:4658-4663(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-947 / MGAS5005 / Serotype M1;
RX PubMed=16088826; DOI=10.1086/432514;
RA Sumby P., Porcella S.F., Madrigal A.G., Barbian K.D., Virtaneva K.,
RA Ricklefs S.M., Sturdevant D.E., Graham M.R., Vuopio-Varkila J., Hoe N.P.,
RA Musser J.M.;
RT "Evolutionary origin and emergence of a highly successful clone of serotype
RT M1 group A Streptococcus involved multiple horizontal gene transfer
RT events.";
RL J. Infect. Dis. 192:771-782(2005).
CC -!- FUNCTION: Converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-
CC acetylglucosamine-6-phosphate (GlcNAc-6-P). {ECO:0000255|HAMAP-
CC Rule:MF_01235}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-D-glucosamine 6-phosphate = an N-acyl-D-mannosamine
CC 6-phosphate; Xref=Rhea:RHEA:23932, ChEBI:CHEBI:57599,
CC ChEBI:CHEBI:57666; EC=5.1.3.9; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01235};
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 3/5.
CC {ECO:0000255|HAMAP-Rule:MF_01235}.
CC -!- SIMILARITY: Belongs to the NanE family. {ECO:0000255|HAMAP-
CC Rule:MF_01235}.
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DR EMBL; AE004092; AAK33327.1; -; Genomic_DNA.
DR EMBL; CP000017; AAZ50831.1; -; Genomic_DNA.
DR RefSeq; NP_268606.1; NC_002737.2.
DR PDB; 1YXY; X-ray; 1.60 A; A/B=1-234.
DR PDBsum; 1YXY; -.
DR AlphaFoldDB; P65522; -.
DR SMR; P65522; -.
DR STRING; 1314.HKU360_00252; -.
DR PaxDb; P65522; -.
DR EnsemblBacteria; AAK33327; AAK33327; SPy_0251.
DR KEGG; spy:SPy_0251; -.
DR KEGG; spz:M5005_Spy0212; -.
DR PATRIC; fig|160490.10.peg.220; -.
DR HOGENOM; CLU_086300_1_0_9; -.
DR OMA; QALGFDC; -.
DR UniPathway; UPA00629; UER00682.
DR EvolutionaryTrace; P65522; -.
DR Proteomes; UP000000750; Chromosome.
DR GO; GO:0047465; F:N-acylglucosamine-6-phosphate 2-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0009385; F:N-acylmannosamine-6-phosphate 2-epimerase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006051; P:N-acetylmannosamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IEA:UniProtKB-UniPathway.
DR CDD; cd04729; NanE; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01235; ManNAc6P_epimer; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR007260; NanE.
DR InterPro; IPR011060; RibuloseP-bd_barrel.
DR PANTHER; PTHR36204; PTHR36204; 1.
DR Pfam; PF04131; NanE; 1.
DR SUPFAM; SSF51366; SSF51366; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Isomerase; Reference proteome.
FT CHAIN 1..234
FT /note="Putative N-acetylmannosamine-6-phosphate 2-
FT epimerase"
FT /id="PRO_0000179809"
FT HELIX 7..14
FT /evidence="ECO:0007829|PDB:1YXY"
FT STRAND 19..21
FT /evidence="ECO:0007829|PDB:1YXY"
FT HELIX 38..48
FT /evidence="ECO:0007829|PDB:1YXY"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:1YXY"
FT HELIX 58..65
FT /evidence="ECO:0007829|PDB:1YXY"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1YXY"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:1YXY"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:1YXY"
FT STRAND 103..108
FT /evidence="ECO:0007829|PDB:1YXY"
FT HELIX 120..130
FT /evidence="ECO:0007829|PDB:1YXY"
FT STRAND 135..139
FT /evidence="ECO:0007829|PDB:1YXY"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:1YXY"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:1YXY"
FT TURN 160..163
FT /evidence="ECO:0007829|PDB:1YXY"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:1YXY"
FT HELIX 176..184
FT /evidence="ECO:0007829|PDB:1YXY"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:1YXY"
FT HELIX 198..205
FT /evidence="ECO:0007829|PDB:1YXY"
FT STRAND 210..214
FT /evidence="ECO:0007829|PDB:1YXY"
FT HELIX 216..219
FT /evidence="ECO:0007829|PDB:1YXY"
FT HELIX 221..231
FT /evidence="ECO:0007829|PDB:1YXY"
SQ SEQUENCE 234 AA; 25066 MW; 8BB6746CC9632090 CRC64;
MPDKPTKEKL MEQLKGGIIV SCQALPGEPL YSETGGIMPL MAKAAQEAGA VGIRANSVRD
IKEIQAITDL PIIGIIKKDY PPQEPFITAT MTEVDQLAAL NIAVIAMDCT KRDRHDGLDI
ASFIRQVKEK YPNQLLMADI STFDEGLVAH QAGIDFVGTT LSGYTPYSRQ EAGPDVALIE
ALCKAGIAVI AEGKIHSPEE AKKINDLGVA GIVVGGAITR PKEIAERFIE ALKS
